“Of the three most common vertebrate subtypes, β-crystallins exhibit the widest degree of polydispersity … [and] it is unclear why there is such a high degree of structural complexity within the β-crystallin subtype. … While the direct, physiological relevance of these divalent cations in the lens is still under investigation, our results support that specific isoforms of β-crystallin modulate polydispersity through multiple chemical equilibria and that this native state is disrupted by cation binding.”

Read the paper and find the full list of authors in the Proceedings of the National Academy of Sciences.